| pubmed-article:20074556 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20074556 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:20074556 | lifeskim:mentions | umls-concept:C1419255 | lld:lifeskim |
| pubmed-article:20074556 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:20074556 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:20074556 | lifeskim:mentions | umls-concept:C1739715 | lld:lifeskim |
| pubmed-article:20074556 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20074556 | pubmed:dateCreated | 2010-2-17 | lld:pubmed |
| pubmed-article:20074556 | pubmed:abstractText | Receptor activity-modifying protein 2 (RAMP2) enables calcitonin receptor-like receptor (CRLR) to form an adrenomedullin (AM)-specific receptor. Here we investigated the function of the cytoplasmic C-terminal tail (C-tail) of human (h)CRLR by co-transfecting its C-terminal mutants into HEK-293 cells stably expressing hRAMP2. Deleting the C-tail from CRLR disrupted AM-evoked cAMP production or receptor internalization, but did not affect [(125)I]AM binding. We found that CRLR residues 428-439 are required for AM-evoked cAMP production, though deleting this region had little effect on receptor internalization. Moreover, pretreatment with pertussis toxin (100ng/mL) led to significant increases in AM-induced cAMP production via wild-type CRLR/RAMP2 complexes. This effect was canceled by deleting CRLR residues 454-457, suggesting Gi couples to this region. Flow cytometric analysis revealed that CRLR truncation mutants lacking residues in the Ser/Thr-rich region extending from Ser(449) to Ser(467) were unable to undergo AM-induced receptor internalization and, in contrast to the effect on wild-type CRLR, overexpression of GPCR kinases-2, -3 and -4 failed to promote internalization of CRLR mutants lacking residues 449-467. Thus, the hCRLR C-tail is crucial for AM-evoked cAMP production and internalization of the CRLR/RAMP2, while the receptor internalization is dependent on the aforementioned GPCR kinases, but not Gs coupling. | lld:pubmed |
| pubmed-article:20074556 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20074556 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20074556 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20074556 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:20074556 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:20074556 | pubmed:author | pubmed-author:KitamuraKazuo... | lld:pubmed |
| pubmed-article:20074556 | pubmed:author | pubmed-author:KuwasakoKenji... | lld:pubmed |
| pubmed-article:20074556 | pubmed:author | pubmed-author:KatoJohjiJ | lld:pubmed |
| pubmed-article:20074556 | pubmed:author | pubmed-author:NagataSayakaS | lld:pubmed |
| pubmed-article:20074556 | pubmed:author | pubmed-author:HikosakaTomom... | lld:pubmed |
| pubmed-article:20074556 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20074556 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:20074556 | pubmed:volume | 392 | lld:pubmed |
| pubmed-article:20074556 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20074556 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20074556 | pubmed:pagination | 380-5 | lld:pubmed |
| pubmed-article:20074556 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:20074556 | pubmed:meshHeading | pubmed-meshheading:20074556... | lld:pubmed |
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| pubmed-article:20074556 | pubmed:meshHeading | pubmed-meshheading:20074556... | lld:pubmed |
| pubmed-article:20074556 | pubmed:meshHeading | pubmed-meshheading:20074556... | lld:pubmed |
| pubmed-article:20074556 | pubmed:meshHeading | pubmed-meshheading:20074556... | lld:pubmed |
| pubmed-article:20074556 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20074556 | pubmed:articleTitle | Function of the cytoplasmic tail of human calcitonin receptor-like receptor in complex with receptor activity-modifying protein 2. | lld:pubmed |
| pubmed-article:20074556 | pubmed:affiliation | Frontier Science Research Center, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan. kuwasako@fc.miyazaki-u.ac.jp | lld:pubmed |
| pubmed-article:20074556 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20074556 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:10203 | entrezgene:pubmed | pubmed-article:20074556 | lld:entrezgene |
| entrez-gene:10266 | entrezgene:pubmed | pubmed-article:20074556 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20074556 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20074556 | lld:entrezgene |
